Universally conserved isoasparylation sustains ribosome biogenesis and function
Abstract
All living beings use ribosomes to synthesize proteins from α-amino acids. Inherited from our common ancestor, a few universally conserved ribosome biogenesis steps, introducing essential ribosomal RNA modifications, have survived to our days. However, it was unknown whether similar primordial core mechanisms could also target ribosomal proteins. Here we show that the assembly and the function of ribosomes depend on the installation of an unusual β-amino acid, isoaspartate, within the ribosomal protein uS11. In bacteria, mitochondria, and plastids, this modification is catalyzed by the metzincin-like hydrolase YbeY, whereas in archaea and eukaryotes, it is introduced by the atypical kinase Fap7. The formation of this strategically positioned isoaspartate enables correct maturation of the small ribosomal subunit to support protein synthesis and normal cell physiology.
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BibTeX
@misc{bonnettaz2026universally,
title = {{Universally conserved isoasparylation sustains ribosome biogenesis and function}},
author = {Bruno Bonnettaz and Anna Smirnova and Marlene Vayssieres and Lila Delbos and Emilie Zelie and Zaineb Kammoun and Yelda Abou Khalil and Mengmeng Zhang and Wang-Qing Liu and Michel Vidal and Johana Chicher and Lauriane Kuhn and Philippe Hammann and Lola Alez-Martin and Tessa Reinert and Nicolas Arnaud and Yannis-Nicolas Francois and Magali Blaud and Nicolas Leulliot and Alexandre Smirnov},
howpublished = {HAL},
year = {2026},
month = aug,
doi = {10.64898/2026.08.26.747345},
url = {https://hal.science/hal-05740499v1},
note = {CC BY 4.0},
}
RIS
TY - UNPB
TI - Universally conserved isoasparylation sustains ribosome biogenesis and function
AU - Bruno Bonnettaz
AU - Anna Smirnova
AU - Marlene Vayssieres
AU - Lila Delbos
AU - Emilie Zelie
AU - Zaineb Kammoun
AU - Yelda Abou Khalil
AU - Mengmeng Zhang
AU - Wang-Qing Liu
AU - Michel Vidal
AU - Johana Chicher
AU - Lauriane Kuhn
AU - Philippe Hammann
AU - Lola Alez-Martin
AU - Tessa Reinert
AU - Nicolas Arnaud
AU - Yannis-Nicolas Francois
AU - Magali Blaud
AU - Nicolas Leulliot
AU - Alexandre Smirnov
PY - 2026
DA - 2026/08/27
PB - HAL
DO - 10.64898/2026.08.26.747345
UR - https://hal.science/hal-05740499v1
AB - All living beings use ribosomes to synthesize proteins from α-amino acids. Inherited from our common ancestor, a few universally conserved ribosome biogenesis steps, introducing essential ribosomal RNA modifications, have survived to our days. However, it was unknown whether similar primordial core mechanisms could also target ribosomal proteins. Here we show that the assembly and the function of ribosomes depend on the installation of an unusual β-amino acid, isoaspartate, within the ribosomal protein uS11. In bacteria, mitochondria, and plastids, this modification is catalyzed by the metzincin-like hydrolase YbeY, whereas in archaea and eukaryotes, it is introduced by the atypical kinase Fap7. The formation of this strategically positioned isoaspartate enables correct maturation of the small ribosomal subunit to support protein synthesis and normal cell physiology.
ER -